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. 2021 Apr 23;10(5):930. doi: 10.3390/foods10050930

Table 4.

The potential of six individual polyphenols at 0.1 and 1 mg/mL towards the inhibition (%) of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activities.

Standards AChE % Inhibition BChE % Inhibition
0.1 mg/mL 1 mg/mL 0.1 mg/mL 1 mg/mL
Ferulic A. 1.0 ± 0.9 b 15.4 ± 0.1 a b 14.6 ± 1 a b 27.2 ± 0.9 a b
p-Coumaric A. 5.2 ± 0.4 a 14.4 ± 0.5 b c 6.4 ± 0.6 b 22.1 ± 1.3 b c
Catechin 3.8 ± 1.1 ab 14.9 ± 0.2 a b 12.2 ± 0.6 a b 31.6 ± 0.4 a b
4-Hydroxybenzoic A. 1.0 ± 0.2 b 5.2 ± 0.9 c n.d. 11.9 ± 0.6 b c
Caffeic A. 3.3 ± 0.4 a b 25.5 ± 0.2 a 15.4 ± 1.3a 52.3 ± 0.8 a
Protocatechuic A. n.d. 13.8 ± 0.7 b c n.d. 7.6 ± 2.4 c
Blends TPC
μgGAE/mg
SQP
μg/mg
AChE
%Inhibition
BChE
%Inhibition
FP EtOAc1 260.6 ± 11.9 a b 1000 n.d. 16.7 ± 1.5 a
BP DE1 243.8 ± 1.4 b 1000 11.1 ± 0.6 a 9.9 ± 0.2 b
BP EtOAc3 267.4 ± 8.4 a 1000 8.3 ± 0.1 a 11.2 ± 1.1 a b

Three blends (FP EtOAc1, BP DE1, BP EtOAc3), that mimic the polyphenol content in the BSG fractions with the highest Total phenolic content (TPC) and sum of quantified polyphenols (SQP) were tested as well. The values reported for each AChE and BChE at specific concentrations with their individual polyphenols bearing different letters (a, b, c) are significantly different (p < 0.05) from each other. n.d. = not detected.